The tissue form of the atomic resolution of RNaseP sub-bases in space in eukaryotes.

Recently, Li Guohui, a researcher at the National Key Laboratory of Molecular Reaction Dynamics at the Dalian Institute of Chemical Physics of the Chinese Academy of Sciences, and Lei Ming, a professor at the Institute of Precision Medicine of Shanghai Jiaotong University, published the latest research results of "Insight Structural Into v. terreved" in collaboration with co-authors of the international academic journal Science.
Ribonuclease (RNase) P is an ancient nucleic acid endoenzyme that is widely found in all living organisms.
RNaseP promotes tRNA maturation by cutting the pre-tRNA5' end sequence, a process that plays an important role in protein synthesis and maintaining cellular function.
esonucleoum RNaseP is an important biomolecular machine consisting of a single-stranded RNA molecule and a dozen protein complexes.
in this study, the Thunder team successfully parsed the structure of the yeast endogenous RNaseP whole enzyme and its substrate pre-tRNA, which reveals the tissue form of the atomic resolution of RNaseP subcells in the eukaryotic organisms.
Li Guohui's team revealed that different constituent proteins have different effects on the stability of different parts of the nuclease itself, and combined with QM/MM/MD simulation and free energy calculation analyzed the catalytic reaction mechanism of RNaseP, and proposed the SN2 reaction model of water molecule-mediated double magnesium ion catalysis, which further expounded the catalytic microsis of this class of ancient nuclear enzymes.
the study not only clearly understands the mature molecular mechanisms of eludal RNaseP catalytic substrate tRNA precursor cutting, but also provides new understanding of the catalytic cosyness of RNA-based riboprotein complexes, the molecular identification mechanism of the substrate tRNA, and the biological evolution of RNA nucleases.
the research work has been specially funded by the National Natural Science Foundation of China and the Chinese Academy of Sciences.
Source: Dalian Institute of Chemical Physics.